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P21550 (ENOB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name=MSE
Skeletal muscle enolase
Gene names
Name:Eno3
Synonyms:Eno-3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to have a function in striated muscle development and regeneration. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and ALDO. Also binds PLG and troponin, in vitro. Interacts with PNKD By similarity. Ref.9

Subcellular location

Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity. Ref.10

Tissue specificity

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, the fiber-type order of ENO3 expression is IIB > IIX > IIA > I. Ref.10

Developmental stage

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In hindleg muscle, first expressed at E15 after which, levels increase sharply between E15 and E17. A steep prenatal rise in expression accompanies the formation of secondary myofibers and the development of innervation. High levels continue throughout newborn and adult stages. Beginning at postnatal day 5, a second sharp increase in expression correlates with the definitive specialization of the myofibers. Later in development, mainly expressed in fast-twitch fibers. In cardiac muscle, first expressed in the embryo in the cardiac tube. Ref.8 Ref.9

Induction

Levels decrease in degenerating myofibers, and increase with their regeneration. Ref.11

Sequence similarities

Belongs to the enolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Beta-enolase HAMAP-Rule MF_00318
PRO_0000134108

Regions

Region370 – 3734Substrate binding By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding2451Magnesium By similarity
Metal binding2931Magnesium By similarity
Metal binding3181Magnesium By similarity
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict234 – 2352AG → NA in AAA37554. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P21550 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A1F757D83709D2B8

FASTA43447,025
        10         20         30         40         50         60 
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKARYLGK 

        70         80         90        100        110        120 
GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 

       190        200        210        220        230        240 
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AVFAGRKFRN PKAK 

« Hide

References

« Hide 'large scale' references
[1]Lamande N., Brosset S., Keller A., Lucas M., Lazar M.
Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: BALB/c and Swiss Webster.
Tissue: Liver and Skeletal muscle.
[2]"Beta-enolase is a marker of human myoblast heterogeneity prior to differentiation."
Peterson C.A., Cho M., Rastinejad F., Blau H.M.
Dev. Biol. 151:626-629(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Colon.
[5]Lubec G., Kang S.U., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Murine muscle-specific enolase: cDNA cloning, sequence, and developmental expression."
Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F., Legault-Demare L., Lazar M.
Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
[7]"Activation of the gene encoding the glycolytic enzyme beta-enolase during early myogenesis precedes an increased expression during fetal muscle development."
Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M., Lazar M.
Mech. Dev. 38:41-54(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION DURING MYOGENESIS.
[8]"Differential expression of alpha- and beta-enolase genes during rat heart development and hypertrophy."
Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F., Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.
Am. J. Physiol. 269:H1843-H1851(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[9]"Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
[10]"Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"Differential modulation of alpha, beta and gamma enolase isoforms in regenerating mouse skeletal muscle."
Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H., Keller A.
Eur. J. Biochem. 267:3735-3743(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPRESSION REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61600 Genomic DNA. Translation: CAA43797.1.
X57747 mRNA. Translation: CAA40913.1.
X62667 mRNA. Translation: CAA44540.1.
AK002485 mRNA. Translation: BAB22137.1.
BC013460 mRNA. Translation: AAH13460.1.
M20745 mRNA. Translation: AAA37554.1.
PIRNOMSB. S17109.
RefSeqNP_001129534.1. NM_001136062.2.
NP_001263214.1. NM_001276285.1.
NP_031959.1. NM_007933.3.
XP_006532225.1. XM_006532162.1.
XP_006537193.1. XM_006537130.1.
UniGeneMm.251322.
Mm.491763.

3D structure databases

ProteinModelPortalP21550.
SMRP21550. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199453. 2 interactions.
IntActP21550. 4 interactions.
MINTMINT-1855839.

PTM databases

PhosphoSiteP21550.

2D gel databases

SWISS-2DPAGEP21550.
UCD-2DPAGEP21550.

Proteomic databases

PaxDbP21550.
PRIDEP21550.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
ENSMUST00000170716; ENSMUSP00000128714; ENSMUSG00000060600.
GeneID13808.
KEGGmmu:13808.
UCSCuc007jvx.2. mouse.

Organism-specific databases

CTD2027.
MGIMGI:95395. Eno3.

Phylogenomic databases

eggNOGCOG0148.
GeneTreeENSGT00550000074560.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP21550.
KOK01689.
OMAGELYKNF.
PhylomeDBP21550.
TreeFamTF300391.

Enzyme and pathway databases

BRENDA4.2.1.11. 3474.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP21550.
BgeeP21550.
CleanExMM_ENO3.
GenevestigatorP21550.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284592.
PROP21550.
SOURCESearch...

Entry information

Entry nameENOB_MOUSE
AccessionPrimary (citable) accession number: P21550
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot